Discrimination of class I CPD photolyase from blue light photoreceptors by single methionine residue
Yuji Miyazawa 1, Hirotaka Nishioka 2, Kei Yura 3 and Takahisa Yamato 1*
1 Nagoya Univ
2 Meijo Univ
3 Japan Atomic Energy Agency
* To whom correspondence should be addressed. E-mail: yamato{at}phys.nagoya-u.ac.jp.
Submitted on August 7, 2007
Revised on August 29, 2007
Accepted on 5 November 2007
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Abstract |
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DNA photolyase recognizes UV-damaged DNA and breaks improperly formed covalent bonds within the cyclobutane pyrimidine dimer (CPD) by light-activated electron transfer reaction between the flavin adenine dinucleotide (FADH-), the electron donor, and CPD, the electron acceptor. Theoretical analysis of the electron tunneling pathways of the DNA photolyase derived from Anacystis nidulans can reveal the active role of the protein environment in the electron transfer reaction. Here, we report the unexpectedly important role of the single methionine residue, Met353, where busy trafficking of electron tunneling currents is observed. The amino acid conservation pattern of Met353 in the homologous sequences perfectly correlates with experimentally verified annotation as photolyases. The bioinformatics sequence analysis also suggests that the residue plays a pivotal role in biological function. Consistent findings from different disciplines of computational biology strongly suggest the pivotal role of Met353 in the biological function of DNA photolyase.
Key Words:
amino acid conservation, electron transfer, molecular dynamics, photorepair
